P20240 · OTE_DROME
- ProteinOtefin
- GeneOte
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids424 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Inner nuclear membrane protein (PubMed:18410727, PubMed:2186029, PubMed:22751930, PubMed:9199347).
Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis (PubMed:22751930, PubMed:9199347).
Essential for differentiation of certain tissues and the maintenance of progenitor cell populations (PubMed:18410727, PubMed:23806619, PubMed:24700158, PubMed:27174470).
Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche (PubMed:18410727, PubMed:23806619, PubMed:27174470).
This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation (PubMed:18410727, PubMed:23806619).
During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1 (PubMed:24700158).
Also has a redundant but important role with bocks during larval development (PubMed:24700158).
Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis (PubMed:22751930, PubMed:9199347).
Essential for differentiation of certain tissues and the maintenance of progenitor cell populations (PubMed:18410727, PubMed:23806619, PubMed:24700158, PubMed:27174470).
Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche (PubMed:18410727, PubMed:23806619, PubMed:27174470).
This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation (PubMed:18410727, PubMed:23806619).
During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1 (PubMed:24700158).
Also has a redundant but important role with bocks during larval development (PubMed:24700158).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | centrosome | |
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | endomembrane system | |
Cellular Component | nuclear envelope lumen | |
Cellular Component | nuclear inner membrane | |
Cellular Component | nuclear membrane | |
Cellular Component | nuclear periphery | |
Cellular Component | nucleoplasm | |
Cellular Component | spindle pole | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | transcription corepressor activity | |
Biological Process | cell division | |
Biological Process | germ-line stem cell population maintenance | |
Biological Process | germ-line stem-cell niche homeostasis | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | nuclear membrane reassembly | |
Biological Process | oogenesis | |
Biological Process | positive regulation of BMP signaling pathway |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOtefin
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP20240
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Nucleus inner membrane ; Peripheral membrane protein
Note: Component of the spindle envelope during early mitotic cycles (PubMed:2186029, PubMed:2517292).
Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles (PubMed:22751930, PubMed:2517292).
At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes (PubMed:22751930, PubMed:2517292).
At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area (PubMed:22751930).
During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body (PubMed:22751930).
At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope (PubMed:9199347).
Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347).
Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles (PubMed:22751930, PubMed:2517292).
At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes (PubMed:22751930, PubMed:2517292).
At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area (PubMed:22751930).
During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body (PubMed:22751930).
At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope (PubMed:9199347).
Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development (PubMed:9199347).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No obvious phenotype (PubMed:18410727, PubMed:23806619, PubMed:24700158).
However females are sterile and aging males become prematurely sterile (PubMed:18410727, PubMed:23806619).
Males and females exhibit a range of defects in their germarium that may be age dependent phenotypes (PubMed:18410727, PubMed:23806619, PubMed:27174470).
Most phenotypes result from defects in germline stem cell (GSC) differentiation that often lead to GSC loss (PubMed:23806619, PubMed:27174470).
Also affects somatic cells of the ovarian stem cell niche, with delayed terminal filament formation and cap cell loss (PubMed:27174470).
In 10 day old males, stem cell niches display a decrease in hub cell number but somatic cyst stem cells are unaffected (PubMed:27174470).
No significant decrease in adult survival, however double mutants with either bocks or Man1 do not survive to the adult stage (PubMed:24700158).
Double bocks and Ote mutant larvae have small brains, their imaginal disks are reduced in size or absent, and only 10% of second-instar larvae reach the pupal stage (PubMed:24700158).
In Ote and MAN1 double mutants, pupal survival and larval development is unaffected (PubMed:24700158).
However females are sterile and aging males become prematurely sterile (PubMed:18410727, PubMed:23806619).
Males and females exhibit a range of defects in their germarium that may be age dependent phenotypes (PubMed:18410727, PubMed:23806619, PubMed:27174470).
Most phenotypes result from defects in germline stem cell (GSC) differentiation that often lead to GSC loss (PubMed:23806619, PubMed:27174470).
Also affects somatic cells of the ovarian stem cell niche, with delayed terminal filament formation and cap cell loss (PubMed:27174470).
In 10 day old males, stem cell niches display a decrease in hub cell number but somatic cyst stem cells are unaffected (PubMed:27174470).
No significant decrease in adult survival, however double mutants with either bocks or Man1 do not survive to the adult stage (PubMed:24700158).
Double bocks and Ote mutant larvae have small brains, their imaginal disks are reduced in size or absent, and only 10% of second-instar larvae reach the pupal stage (PubMed:24700158).
In Ote and MAN1 double mutants, pupal survival and larval development is unaffected (PubMed:24700158).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 54 | Loss of phosphorylation by Cdk1. | ||||
Sequence: S → A | ||||||
Mutagenesis | 63 | Prevents phosphorylation and displays an increase in the number of mitotic cells. | ||||
Sequence: T → A | ||||||
Mutagenesis | 63 | Phosphomimetic mutant which displays a decrease in the number of mitotic cells. | ||||
Sequence: T → E |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000206151 | 1-424 | Otefin | |||
Sequence: MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKVVEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQKYHIKSKLFIVLLVLLLIGVYYIFY | ||||||
Modified residue | 44 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 50 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 54 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 63 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 152 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 192 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 198 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 321 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 324 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 326 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 358 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 378 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 385 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Thr-63 by aurA may be required for exit from mitosis (PubMed:22751930).
May be phosphorylated by Cdk1 and Pka-C1 (PubMed:9199347).
May be phosphorylated by Cdk1 and Pka-C1 (PubMed:9199347).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in all cell types of the germarium and testis (PubMed:18410727, PubMed:27174470).
Expressed in nurse cells, follicle cells and oocytes (PubMed:9199347).
Expressed in nurse cells, follicle cells and oocytes (PubMed:9199347).
Developmental stage
Relatively high levels of expression in eggs and 1st instar larvae compared to pupal and adult stages, with weak expression in 2nd instar larvae (at protein level) (PubMed:16439308).
Expressed throughout development in all somatic cells (PubMed:9199347).
Highest levels of expression in embryos and weak expression in larvae and adults (PubMed:2186029, PubMed:9199347).
Expressed throughout development (at protein level) (PubMed:2517292).
Expressed throughout development in all somatic cells (PubMed:9199347).
Highest levels of expression in embryos and weak expression in larvae and adults (PubMed:2186029, PubMed:9199347).
Expressed throughout development (at protein level) (PubMed:2517292).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-30 | LEM | ||||
Sequence: MADVDDFDSLSNAELRAKMLAQGLPNIPVT | ||||||
Region | 1-50 | Required for binding to Med and germline stem cell maintenance | ||||
Sequence: MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQAS | ||||||
Region | 42-186 | Disordered | ||||
Sequence: RASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREEN | ||||||
Motif | 92-99 | Nuclear localization signal | ||||
Sequence: ATKARRTI | ||||||
Compositional bias | 99-132 | Basic and acidic residues | ||||
Sequence: ITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPV | ||||||
Compositional bias | 141-159 | Polar residues | ||||
Sequence: PAAQPVQTRRTSTSSGSER | ||||||
Region | 259-278 | Disordered | ||||
Sequence: PSVPSARAQTTSSTRSYDYA | ||||||
Compositional bias | 262-278 | Polar residues | ||||
Sequence: PSARAQTTSSTRSYDYA | ||||||
Region | 271-400 | Required for binding to Med | ||||
Sequence: STRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQK | ||||||
Region | 400-424 | Essential for nuclear membrane localization and germline stem cell maintenance | ||||
Sequence: KYHIKSKLFIVLLVLLLIGVYYIFY | ||||||
Region | 406-424 | Essential for nuclear membrane localization | ||||
Sequence: KLFIVLLVLLLIGVYYIFY |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length424
- Mass (Da)46,584
- Last updated2004-02-02 v2
- Checksum51E3A83284F7988B
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 99-132 | Basic and acidic residues | ||||
Sequence: ITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPV | ||||||
Sequence conflict | 116 | in Ref. 1; CAA35530 | ||||
Sequence: I → V | ||||||
Sequence conflict | 121 | in Ref. 1; CAA35530 | ||||
Sequence: D → E | ||||||
Sequence conflict | 128 | in Ref. 1; CAA35530 | ||||
Sequence: S → P | ||||||
Sequence conflict | 141 | in Ref. 1; CAA35530 | ||||
Sequence: P → S | ||||||
Compositional bias | 141-159 | Polar residues | ||||
Sequence: PAAQPVQTRRTSTSSGSER | ||||||
Sequence conflict | 151 | in Ref. 1; CAA35530 | ||||
Sequence: T → S | ||||||
Sequence conflict | 186 | in Ref. 1; CAA35530 | ||||
Sequence: N → K | ||||||
Sequence conflict | 254 | in Ref. 1; CAA35530 | ||||
Sequence: A → S | ||||||
Compositional bias | 262-278 | Polar residues | ||||
Sequence: PSARAQTTSSTRSYDYA | ||||||
Sequence conflict | 292 | in Ref. 1; CAA35530 | ||||
Sequence: T → H | ||||||
Sequence conflict | 344 | in Ref. 1; CAA35530 | ||||
Sequence: A → S | ||||||
Sequence conflict | 412 | in Ref. 1; CAA35530 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAF57722.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051940 EMBL· GenBank· DDBJ | AAK93364.1 EMBL· GenBank· DDBJ | mRNA | ||
X17495 EMBL· GenBank· DDBJ | CAA35530.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |